Published December 1993
| Version public
Journal Article
Dinitrogen Reduction by Nitrogenase: If N_2 Isn't Broken, It Can't be Fixed
Abstract
Nitrogenase consists of two component metalloproteins, the iron protein and molybdenum-iron protein, which together catalyze the ATP-dependent reduction of dinitrogen to ammonia during biological nitrogen fixation. With the recent crystal structure determinations of both proteins, a structural framework is now available for interpreting the mechanism of nitrogenase at the molecular level.
Additional Information
© 1993 Current Biology Ltd. This work was supported by National Institutes of Health grant GM45162 and National Science Foundation grant DMB91-18689. The contributions of J. Kim, MM Georgiadis, BT Hsu, H Komiya, MK Chan, D Woo, JL Schlessman, MW Day, AJ Chirino, MHB Stowell and L Joshua-Tor to the crystallographic work at Caltech, along with most enjoyable discussions with JB Howard, made this review possible.Additional details
Additional titles
- Alternative title
- Dinitrogen Reduction by Nitrogenase: If N2 Isn't Broken, It Can't be Fixed
Identifiers
- Eprint ID
- 54450
- Resolver ID
- CaltechAUTHORS:20150205-141635090
Funding
- NIH
- GM45162
- NSF
- DMB91-18689
Dates
- Created
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2015-02-08Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field